Domains and Maturation Processes That Regulate the Activity of ADAMTS-2, a Metalloproteinase Cleaving the Aminopropeptide of Fibrillar Procollagens Types I–III and V
Open Access
- 1 October 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (41) , 34397-34408
- https://doi.org/10.1074/jbc.m506458200
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Novel Types of Mutation Responsible for the Dermatosparactic Type of Ehlers–Danlos Syndrome (Type VIIC) and Common Polymorphisms in the ADAMTS2 GeneJournal of Investigative Dermatology, 2004
- Biosynthetic Processing of the Pro-α1(V)Pro-α2(V)Pro-α3(V) Procollagen HeterotrimerPublished by Elsevier ,2004
- Transforming Growth Factor-β Induces Secretion of Activated ADAMTS-2Journal of Biological Chemistry, 2003
- Cloning and Characterization of ADAMTS-14, a Novel ADAMTS Displaying High Homology with ADAMTS-2 and ADAMTS-3Journal of Biological Chemistry, 2002
- Procollagen II Amino Propeptide Processing by ADAMTS-3Journal of Biological Chemistry, 2001
- Type V collagen: heterotypic type I/V collagen interactions in the regulation of fibril assemblyMicron, 2000
- Human Ehlers-Danlos Syndrome Type VII C and Bovine Dermatosparaxis Are Caused by Mutations in the Procollagen I N-Proteinase GeneAmerican Journal of Human Genetics, 1999
- Bone Morphogenetic Protein-1 Processes the NH2-terminal Propeptide, and a Furin-like Proprotein Convertase Processes the COOH-terminal Propeptide of pro-α1(V) CollagenPublished by Elsevier ,1998
- Another look at collagen V and XI moleculesMatrix Biology, 1995
- Evidence for a relationship between Ehlers–Danlos type VII C in humans and bovine dermatosparaxisNature Genetics, 1992